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Structural Research of Beta-sheet Pore-forming Toxins/Attack Complexes

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Beta-sheet pore-forming toxins (β-PFTs) are a group of proteins that form pores in cell membranes through a series of conformational changes. β-strands are responsible for forming β-barrel and insert into the membrane. They are a widespread class of bacterial toxins and are known to cause various diseases. β-PFTs have been found in many bacteria, such as Listeria and Staphylococcus aureus. They are also involved in the virulence of some pathogens, making them an important target for the development of new treatments. Attack complexes are a subset of β-PFTs that work together as multi-subunit assemblies to create pores in host cell membranes, allowing for pathogenic organisms to enter and damage the host.

A recent study explores the structure of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile, using cryo-electron microscopy (cryo-EM). The study provides insights into the mechanism of the binary toxin complex, observing that CDTb forms a barrel-shaped pore in the host cell membrane, with a central channel that allows for the translocation of CDTa. CDTa binds to the pore in a specific orientation, which is critical for its translocation into the host cell.

Cryo-EM density maps of CDTa-bound CDTb-pores.Figure 1. Cryo-EM density maps of CDTa-bound CDTb-pores. (Kawamoto A, et al., 2022)

ProteinOrganismMethodResolutionPDB Entry ID
α-hemolysinStaphylococcus aureusX-ray diffraction1.89 Å7AHL
M113F mutant of α-hemolysin (expressed in Staphylococcus aureus)Staphylococcus aureusX-ray diffraction2.10 Å3M2L
α-hemolysin (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.30 Å3ANZ
α-hemolysin heptamer, C14-bound (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.35 Å6U49
γ-hemolysin composed of LukF and Hlg2 (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.50 Å3B07
γ-hemolysin prepore (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.99 Å4P1Y
LukF component of γ-hemolysin (expressed in E. coli)Staphylococcus aureusX-ray diffraction1.90 Å1LKF
LUK prepore formed from LukF & LukS (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.40 Å4P1X
LukGH octamer (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.80 Å4TW1
Leukocidin (LukFG) in complex with mouse CD11b I-domain (CD11b-I) (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.29 Å6RHV
LukD, no ligand (expressed in E. coli)Staphylococcus aureusX-ray diffraction1.75 Å6U33
leukotoxin LukE (expressed in E. coli)Staphylococcus aureusX-ray diffraction1.46 Å7P8T
Panton-Valentine leukocidin (PVL) with bound C14PC (expressed in E. coli)Staphylococcus aureusX-ray diffraction2.04 Å6U3Y
NetB Necrotic B-like enteritis toxin (expressed in E. coli)Clostridium perfringensX-ray diffraction3.90 Å4H56
Perfringolysin O (PFO) protomer (expressed in E. coli)Clostridium perfringensX-ray diffraction2.20 Å1PFO
Anthrax Protective Antigen (PA) and Lethal Factor (LF) Prechannel Complex (expressed in E. coli)Bacillus anthracisX-ray diffraction3.10 Å3KWV
Anthrax protective antigen pore (expressed in E. coli)Bacillus anthracisCryo-EM single particle analysis2.90 Å3J9C
Anthrax octamer prechannel bound to full-length edema factor (EF) (expressed in E. coli)Bacillus anthracisCryo-EM single particle analysis3.30 Å6VRA
Anthrax protective antigen pore translating N-terminal of LF (expressed in E. coli)Bacillus anthracisCryo-EM single particle analysis3.30 Å7KXR
Lymphocyte perforin monomer (expressed in Spodoptera frugiperda)Mus musculusX-ray diffraction2.75 Å3NSJ
Lymphocyte perforin pore (expressed in Spodoptera frugiperda)Mus musculusCryo-EM single particle analysis4.00 Å7PAG
Macrophage-expressed gene 1 (MPEG1/Perforin-2), wild-type soluble pre-pore (expressed in Spodoptera frugiperda)Homo sapiensCryo-EM single particle analysis3.49 Å6U23
Macrophage-expressed gene 1 (MPEG1/Perforin-2), pore in ring form (expressed in HEK293 cells)Mus musculusCryo-EM single particle analysis3.00 Å8A1D
Cytolysin pore-forming toxin (expressed in E. coli)Vibrio choleraeX-ray diffraction2.88 Å3O44
Cytolysin pore-forming toxin protomer (expressed in E. coli)Vibrio choleraeX-ray diffraction2.30 Å1XEZ
Streptolysin O pore-forming toxin (expressed in E. coli)Streptococcus pyogenesX-ray diffraction2.10 Å4HSC
Aerolysin pore-forming toxin Y221G mutant (expressed in Aeromonas salmonicida)Aeromonas hydrophilaX-ray diffraction2.88 Å3C0M
Monalysin pore-forming toxin, cleaved form (expressed in E. coli)Pseudomonas entomophilaX-ray diffraction1.70 Å4MKO
poly-C9 component of the complement membrane attack ComplexHomo sapiensCryo-EM single particle analysis6.70 Å5FMW
poly-C9 component of the complement membrane attack Complex (expressed in Expi293 cells)Homo sapiensCryo-EM single particle analysis3.90 Å6DLW
Membrane attack complex (MAC) in open conformationHomo sapiensCryo-EM single particle analysis5.60 Å6H03
3C9-sMAC Complement membrane attack complex packaged for clearanceHomo sapiensCryo-EM single particle analysis3.54 Å7NYC
Monomeric C9 component of the complement membrane attack Complex (expressed in Expi293 cells)Mus musculusX-ray diffraction2.20 Å6CXO
Lysenin Pore complex (expressed in E. coli)Eisenia fetidaCryo-EM single particle analysis3.10 Å5GAQ
ILYml Cholesterol-dependent cytolysin, CD59-responsive (expressed in E. coli)Streptococcus intermediusX-ray diffraction2.89 Å5IMW
VLYml Cholesterol-dependent cytolysin, CD-59 responsive, bound to CD59D22A (expressed in E. coli)Gardnerella vaginalisX-ray diffraction2.40 Å5IMY
Pneumolysin (PLY) complex (expressed in E. coli)Streptococcus pneumoniaeCryo-EM single particle analysis4.50 Å5LY6
Epsilon toxin (Etx) (expressed in E. coli)Clostridium perfringensCryo-EM single particle analysis3.20 Å6RB9
Binary iota toxin complex Ib pore (expressed in E. coli)Clostridium perfringensCryo-EM single particle analysis2.90 Å6KLX
Binary toxin translocase CDTb in asymmetric tetradecamer conformation (expressed in E. coli)Clostridioides difficileCryo-EM single particle analysis2.80 Å6UWR
Binary toxin translocase CDTb with CDTa long-stem pore (expressed in E. coli)Clostridioides difficileCryo-EM single particle analysis2.64 Å7VNN

Table 1. Structural Research of Beta-sheet Pore-forming Toxins/Attack Complexes.

Creative Biostructure is a leading provider of structural biology services that can assist researchers in advancing their understanding of these complex proteins. We offer a range of services that can help researchers determine the structure of β-PFTs and their attack complexes, including X-ray crystallography, NMR spectroscopy, and cryo-EM.

If you are interested in exploring the structural research of β-PFT or other membrane proteins, please don't hesitate to contact us. Our comprehensive structural biology services allow clients to leverage our expertise, beginning with protein expression and purification through to structure determination.

References

  1. Kawamoto A, et al. Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile. Nature Communications. 2022, 13(1): 6119.
  2. Trstenjak N, et al. Molecular mechanism of leukocidin GH–integrin CD11b/CD18 recognition and species specificity. Proceedings of the National Academy of Sciences. 2020, 117(1): 317-327.
  3. Lambey P, et al. Structural insights into recognition of chemokine receptors by Staphylococcus aureus leukotoxins. Elife. 2022, 11: e72555.

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